Electrosyneresis (ES) was employed for the detection of enzyme-linked immunoglobulin.
ES is said to be unsatisfactory for detecting the cathodally migrating proteins such as immunoglobulins. When ES was carried out using the electrophoretic system in which serum application point was located in the middle of γ-globulin region, precipitin lines of IgA and of IgM could be formed on the anodic site of antigen (serum) application point and those of IgG on the cathodic and anodic site.
Non-precipitated enzyme was removed from the gel by pressing and enzyme staining was subsequently performed.
The method described here offers the following advantages: (1) The procedure is rapid; it takes 40min for the development of immunoprecipitin line and 30min for the removal of non-precipitated enzyme. (2) The detection of immunoglobulin is sensitive because it is based on ES. (3) Antiserum needed is minimal.
We compared the sensitivity of detecting LDH-linked immunoglobulins by ES, immunoelectrophoresis (IEP) and immunofixation (IF) using 28 sera with anomalous isoenzyme pattern. The frequency of identifing IgA was almost same in all methods, however, the number of IgG and light chains detected by ES was twice that of IF method and the sensitivity of IEP was intermediate that of ES and IF procedure.

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Enzyme activities and isoenzyme patterns were studied in the myocardial homogenates of rats. The remarkable high activities were observed on GOT, LDH and CK. In myocardial LDH-isozyme of normal rats, the sum of LDH₁ and LDH₂ accounted for 80% of the total activity. In myocardial CK-isozyme of normal rats, activities of CK-MM and CK-MB were 80% and 16% of the total, respectively. Weak activity of mitochondrial CK was observed in the cathode side to CK-MM. In myocardial hypertrophies produced by the thyroxine treatment, decrease in LDH₁ and increase in LDH₂ were observed, while, in the hypoxic hearts produced by low oxygen loading, increase in LDH₃ were recognized in addition to the change in myocardial hypertrophies. The results seem to show that H-subunits in myocardial LDH-isozyme shift toward M-subunits in anaerobic conditions.

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